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Crosstalk between insulin-like growth factor (IGF) receptor and integrins through direct integrin binding to IGF1

Cytokine & growth factor reviews, 2017-04, Vol.34, p.67-72

2017

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Stromal cell-derived factor-1 (CXCL12) activates integrins by direct binding to an allosteric ligand-binding site (site 2) of integrins without CXCR4

Biochemical journal, 2018-02, Vol.475 (4), p.723-732

2018

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CD40L Activates Platelet Integrin αIIbβ3 by Binding to the Allosteric Site (Site 2) in a KGD-Independent Manner and HIGM1 Mutations Are Clustered in the Integrin-Binding Sites of CD40L

Cells (Basel, Switzerland), 2023-07, Vol.12 (15), p.1977

2023

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The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct from the classical RGD-binding site

PloS one, 2014-05, Vol.9 (5), p.e96372-e96372

2014

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Virtual Screening of Protein Data Bank via Docking Simulation Identified the Role of Integrins in Growth Factor Signaling, the Allosteric Activation of Integrins, and P-Selectin as a New Integrin Ligand

Cells (Basel, Switzerland), 2023-09, Vol.12 (18), p.2265

2023

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A dominant-negative FGF1 mutant (the R50E mutant) suppresses tumorigenesis and angiogenesis

PloS one, 2013-02, Vol.8 (2), p.e57927-e57927

2013

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FGF1 Suppresses Allosteric Activation of β3 Integrins by FGF2: A Potential Mechanism of Anti-Inflammatory and Anti-Thrombotic Action of FGF1

Biomolecules (Basel, Switzerland), 2024-07, Vol.14 (8), p.888

2024

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Pro-Inflammatory Chemokines CCL5, CXCL12, and CX3CL1 Bind to and Activate Platelet Integrin αIIbβ3 in an Allosteric Manner

Cells (Basel, Switzerland), 2022-09, Vol.11 (19), p.3059

2022

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Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling

PloS one, 2017-09, Vol.12 (9), p.e0184285-e0184285

2017

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The binding of monomeric C-reactive protein (mCRP) to Integrins αvβ3 and α4β1 is related to its pro-inflammatory action

PloS one, 2014-04, Vol.9 (4), p.e93738-e93738

2014

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Direct Binding of the EGF-like Domain of Neuregulin-1 to Integrins (αvβ3 and α6β4) Is Involved in Neuregulin-1/ErbB Signaling

The Journal of biological chemistry, 2010-10, Vol.285 (41), p.31388-31398

2010

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The heparin-binding domain of VEGF165 directly binds to integrin αvβ3 and VEGFR2/KDR D1: a potential mechanism of negative regulation of VEGF165 signaling by αvβ3

Frontiers in cell and developmental biology, 2024-05, Vol.12, p.1347616-1347616

2024

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The integrin-binding defective FGF2 mutants potently suppress FGF2 signalling and angiogenesis

Bioscience reports, 2017-04, Vol.37 (2)

2017

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Cross-talk between Integrin α6β4 and Insulin-like Growth Factor-1 Receptor (IGF1R) through Direct α6β4 Binding to IGF1 and Subsequent α6β4-IGF1-IGF1R Ternary Complex Formation in Anchorage-independent Conditions

The Journal of biological chemistry, 2012-04, Vol.287 (15), p.12491-12500

2012

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FGF9, a Potent Mitogen, Is a New Ligand for Integrin αvβ3, and the FGF9 Mutant Defective in Integrin Binding Acts as an Antagonist

Cells (Basel, Switzerland), 2024-02, Vol.13 (4), p.307

2024

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Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role in CD40/CD40L Signaling

The Journal of immunology (1950), 2019-09, Vol.203 (5), p.1383-1391

2019

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An Integrin Binding-defective Mutant of Insulin-like Growth Factor-1 (R36E/R37E IGF1) Acts as a Dominant-negative Antagonist of the IGF1 Receptor (IGF1R) and Suppresses Tumorigenesis but Still Binds to IGF1R

The Journal of biological chemistry, 2013-07, Vol.288 (27), p.19593-19603

2013

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A novel fibroblast growth factor-1 (FGF1) mutant that acts as an FGF antagonist

PloS one, 2010-04, Vol.5 (4), p.e10273-e10273

2010

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Insulin-like Growth Factor (IGF) Signaling Requires αvβ3-IGF1-IGF Type 1 Receptor (IGF1R) Ternary Complex Formation in Anchorage Independence, and the Complex Formation Does Not Require IGF1R and Src Activation

The Journal of biological chemistry, 2013-02, Vol.288 (5), p.3059-3069

2013

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Soluble CD40L activates soluble and cell-surface integrin αvβ3, α5β1, and α4β1 by binding to the allosteric ligand-binding site (site 2)

The Journal of biological chemistry, 2021-01, Vol.296, p.100399-100399, Article 100399

2021

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The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3

Biochemical journal, 2017-02, Vol.474 (4), p.589-596

2017

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The C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand

Life science alliance, 2023-07, Vol.6 (7), p.e202201747

2023

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Proinflammatory Secreted Phospholipase A2 Type IIA (sPLA-IIA) Induces Integrin Activation through Direct Binding to a Newly Identified Binding Site (Site 2) in Integrins αvβ3, α4β1, and α5β1

The Journal of biological chemistry, 2015-01, Vol.290 (1), p.259-271

2015

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Direct binding to integrins and loss of disulfide linkage in interleukin-1β (IL-1β) are involved in the agonistic action of IL-1β

The Journal of biological chemistry, 2017-12, Vol.292 (49), p.20067-20075

2017

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Integrins αvβ3 and α4β1 act as coreceptors for fractalkine, and the integrin-binding defective mutant of fractalkine is an antagonist of CX3CR1

The Journal of immunology (1950), 2012-12, Vol.189 (12), p.5809-5819

2012

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Crosstalk between insulin-like growth factor (IGF) receptor and integrins through direct integrin binding to IGF1

Stromal cell-derived factor-1 (CXCL12) activates integrins by direct binding to an allosteric ligand-binding site (site 2) of integrins without CXCR4

CD40L Activates Platelet Integrin αIIbβ3 by Binding to the Allosteric Site (Site 2) in a KGD-Independent Manner and HIGM1 Mutations Are Clustered in the Integrin-Binding Sites of CD40L

The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct from the classical RGD-binding site

Virtual Screening of Protein Data Bank via Docking Simulation Identified the Role of Integrins in Growth Factor Signaling, the Allosteric Activation of Integrins, and P-Selectin as a New Integrin Ligand

A dominant-negative FGF1 mutant (the R50E mutant) suppresses tumorigenesis and angiogenesis

FGF1 Suppresses Allosteric Activation of β3 Integrins by FGF2: A Potential Mechanism of Anti-Inflammatory and Anti-Thrombotic Action of FGF1

Pro-Inflammatory Chemokines CCL5, CXCL12, and CX3CL1 Bind to and Activate Platelet Integrin αIIbβ3 in an Allosteric Manner

Direct integrin binding to insulin-like growth factor-2 through the C-domain is required for insulin-like growth factor receptor type 1 (IGF1R) signaling

The binding of monomeric C-reactive protein (mCRP) to Integrins αvβ3 and α4β1 is related to its pro-inflammatory action

Direct Binding of the EGF-like Domain of Neuregulin-1 to Integrins (αvβ3 and α6β4) Is Involved in Neuregulin-1/ErbB Signaling

The heparin-binding domain of VEGF165 directly binds to integrin αvβ3 and VEGFR2/KDR D1: a potential mechanism of negative regulation of VEGF165 signaling by αvβ3

The integrin-binding defective FGF2 mutants potently suppress FGF2 signalling and angiogenesis

Cross-talk between Integrin α6β4 and Insulin-like Growth Factor-1 Receptor (IGF1R) through Direct α6β4 Binding to IGF1 and Subsequent α6β4-IGF1-IGF1R Ternary Complex Formation in Anchorage-independent Conditions

FGF9, a Potent Mitogen, Is a New Ligand for Integrin αvβ3, and the FGF9 Mutant Defective in Integrin Binding Acts as an Antagonist

Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role in CD40/CD40L Signaling

An Integrin Binding-defective Mutant of Insulin-like Growth Factor-1 (R36E/R37E IGF1) Acts as a Dominant-negative Antagonist of the IGF1 Receptor (IGF1R) and Suppresses Tumorigenesis but Still Binds to IGF1R

A novel fibroblast growth factor-1 (FGF1) mutant that acts as an FGF antagonist

Insulin-like Growth Factor (IGF) Signaling Requires αvβ3-IGF1-IGF Type 1 Receptor (IGF1R) Ternary Complex Formation in Anchorage Independence, and the Complex Formation Does Not Require IGF1R and Src Activation

Soluble CD40L activates soluble and cell-surface integrin αvβ3, α5β1, and α4β1 by binding to the allosteric ligand-binding site (site 2)

The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3

The C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand

Proinflammatory Secreted Phospholipase A2 Type IIA (sPLA-IIA) Induces Integrin Activation through Direct Binding to a Newly Identified Binding Site (Site 2) in Integrins αvβ3, α4β1, and α5β1

Direct binding to integrins and loss of disulfide linkage in interleukin-1β (IL-1β) are involved in the agonistic action of IL-1β

Integrins αvβ3 and α4β1 act as coreceptors for fractalkine, and the integrin-binding defective mutant of fractalkine is an antagonist of CX3CR1

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